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학술발표회초록보기

초록문의 abstract@kcsnet.or.kr

결제문의 member@kcsnet.or.kr

현재 가능한 작업은 아래와 같습니다.
  • 09월 04일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제114회 대한화학회 학술발표회, 총회 및 기기전시회 안내 NSF disassembles a single SNARE complex in one round of ATP turnvoer

등록일
2014년 8월 28일 16시 17분 51초
접수번호
1216
발표코드
BIO1-4 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 10시 : 00분
발표형식
심포지엄
발표분야
생명화학 - Neurodegenerative Diseases in Life Chemistry
저자 및
공동저자
윤태영
한국과학기술원(KAIST) 물리학과, Korea
N-ethylmaleimide-sensitive factor (NSF) and soluble NSF attachment protein (α-SNAP) disassemble the soluble NSF attachment protein receptor (SNARE) complex using ATP hydrolysis (the 20S particle) for recycling of the SNARE proteins. Despite its fundamental importance for sustained membrane traffic, the molecular mechanism by which NSF disassembles the SNARE complex is largely unknown. In this talk, with the observations using two orthogonal techniques of single-molecule fluorescence resonance energy transfer (FRET) and magnetic tweezers, I will show that NSF disassembles a single SNARE complex in only one round of ATP turnover. To realize such a high energy efficiency, α-SNAP destabilizes the C-terminal part of the SNARE motif and tightly connects the SNARE complex and NSF. Like a spring-loaded machine, the NSF hexamer releases its built up tension in a burst within 20 ms to disassemble the SNARE complex essentially in one step. The disassembled SNARE proteins are immediately released from the 20S particle. Our observations unravel how an AAA+ ATPase induces global unwinding of the substrate protein complex, which turns out to be a much more efficient mechanism than processive unwinding.

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